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Chemical modification of amino acids by atmospheric-pressure cold plasma in aqueous solution

Eisuke TakaiFaculty of Pure and Applied Sciences, University of Tsukuba , 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573, JapanTsuyoshi KitamuraDepartment of Chemistry and Materials Engineering, Faculty of Chemistry, Materials and Bioengineering, Kansai University, 3-3-35, Yamate-cho, Suita-shi, Osaka 564-8680, JapanJunpei KuwabaraTsukuba Research Center for Interdisciplinary Materials Science (TIMS), Graduate School of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba 305-8573, JapanSatoshi IkawaTechnology Research Institute of Osaka Prefecture 2-7-1 Ayumino, Izumi, Osaka 594–1157, JapanShunsuke YoshizawaFaculty of Pure and Applied Sciences, University of Tsukuba , 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573, JapanKentaro ShirakiFaculty of Pure and Applied Sciences, University of Tsukuba , 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573, JapanHideya KawasakiDepartment of Chemistry and Materials Engineering, Faculty of Chemistry, Materials and Bioengineering, Kansai University, 3-3-35, Yamate-cho, Suita-shi, Osaka 564-8680, JapanRyuichi ArakawaDepartment of Chemistry and Materials Engineering, Faculty of Chemistry, Materials and Bioengineering, Kansai University, 3-3-35, Yamate-cho, Suita-shi, Osaka 564-8680, JapanKatsuhisa KitanoCenter for Atomic and Molecular Technologies, Graduate School of Engineering, Osaka University, Osaka 565-0871, Japan

2014en

ABI

Annotatsiya

Plasma medicine is an attractive new research area, but the principles of plasma modification of biomolecules in aqueous solution remain elusive. In this study, we investigated the chemical effects of atmospheric-pressure cold plasma on 20 naturally occurring amino acids in aqueous solution. High-resolution mass spectrometry revealed that chemical modifications of 14 amino acids were observed after plasma treatment: (i) hydroxylation and nitration of aromatic rings in tyrosine, phenylalanine and tryptophan; (ii) sulfonation and disulfide linkage formation of thiol groups in cysteine; (iii) sulfoxidation of methionine and (iv) amidation and ring-opening of five-membered rings in histidine and proline. A competitive reaction experiment using 20 amino acids demonstrated that sulfur-containing and aromatic amino acids were preferentially decreased by the plasma treatment. These data provide fundamental information for elucidating the mechanism of protein inactivation for biomedical plasma applications.

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DOI: 10.1088/0022-3727/47/28/285403

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